4ANI: Structural Basis For The Intermolecular Communication Between Dnak And Grpe In The Dnak Chaperone System From Geobacillus Kaustophilus Hta426

The conserved, ATP-dependent bacterial DnaK chaperones process client substrates with the aid of the co-chaperones DnaJ and GrpE. However, in the absence of structural information, how these proteins communicate with each other cannot be fully delineated. For the study reported here, we solved the crystal structure of a full-length Geobacillus kaustophilus HTA426 GrpE homodimer in complex with a nearly full-length G. kaustophilus HTA426 DnaK that contains the interdomain linker (acting as a pseudo-substrate), and the N-terminal nucleotide-binding and C-terminal substrate-binding domains at 4.1-A resolution. Each complex contains two DnaKs and two GrpEs, which is a stoichiometry that has not been found before. The long N-terminal GrpE alpha-helices stabilize the linker of DnaK in the complex. Furthermore, interactions between the DnaK substrate-binding domain and the N-terminal disordered region of GrpE may accelerate substrate release from DnaK. These findings provide molecular mechanisms for substrate binding, processing, and release during the Hsp70 chaperone cycle.
PDB ID: 4ANIDownload
MMDB ID: 99896
PDB Deposition Date: 2012/3/19
Updated in MMDB: 2012/08
Experimental Method:
x-ray diffraction
Resolution: 4.09  Å
Source Organism:
Similar Structures:
Biological Unit for 4ANI: octameric; determined by author and by software (PISA)
Molecular Components in 4ANI
Label Count Molecule
Proteins (8 molecules)
Protein Grpe
Molecule annotation
Chaperone Protein Dnak
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB